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Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1–40).
Open accessAbstract
We reported earlier that the levels of Ca 2+ -dependent metalloproteinases are increased in Alzheimer’s disease (AD) specimens, relative to control specimens. Here we show that these enzymes are forms of the matrix metalloproteinase MMP-9 (EC 3.4.24.35 ) and are expressed in the human hippocampus. Affinity-purified antibodies to MMP-9 labeled pyramidal neurons, but not granular neurons or glial cells. MMP-9 mRNA is expressed in pyramidal neurons, as determined with digoxigenin-labeled MMP-9 riboprobes, and the presence of this mRNA is confirmed with reverse transcriptase PCR. The cellular distribution of MMP-9 is altered in AD because 76% of the total 100 kDa enzyme activity is found in the soluble fraction of control specimens, whereas only 51% is detectable in the same fraction from AD specimens. The accumulated 100 kDa enzyme from AD brain is latent and can be converted to an active form with aminophenylmercuric acetate. MMP-9 also is detected in close proximity to extracellular amyloid plaques. Because a major constituent of plaques is the 4 kDa β-amyloid peptide, synthetic Aβ 1–40 was incubated with activated MMP-9. The enzyme cleaves the peptide at several sites, predominantly at Leu 34 -Met 35 within the membrane-spanning domain. These results establish that neurons have the capacity to synthesize MMP-9, which, on activation, may degrade extracellular substrates such as β-amyloid. Because the latent form of MMP-9 accumulates in AD brain, it is hypothesized that the lack of enzyme activation contributes to the accumulation of insoluble β-amyloid peptides in plaques.
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“Increasing in vitro evidence indicates that some MMPs may play an important role in degrading soluble Ab (sAb), such as secreted MMP-2 and MMP-9 that generate C-terminally truncated Ab fragments and membrane-type MMP-14 that degrades both soluble and fibrillary Ab (29)(30)(31)(32).”
From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [29]
Experimental — accuracy not yet measuredIn the citing paper
“In parallel, a number of these CNS diseases exhibit dysregulated expression of enzymes necessary for PNN cleavage and reorganization (Backstrom et al., 1996; Lorenzl et al., 2003; Rybakowski et al., 2009; Kim et al., 2009; Zhang et al., 2011; Yamamori et al., 2013; Liu et al., 2014; Rankin-Gee et al., 2015; Lepeta et al., 2017).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Backstrom et al., 1996
In the citing paper
“plasma levels of MMP-9 are elevated in AD patients (Backstrom et al., 1996; Lorenzl et al., 2003).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Backstrom et al., 1996
In the citing paper
“MMP-9 is capable of cleaving Aβ in vitro (Backstrom et al., 1996)”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Backstrom et al., 1996
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Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
Diagnosis of Alzheimer's Disease
Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499 · cited 1×
“The diagnosis of AD was confirmed by postmortem neuropathological examination via the diagnostic criteria of the Consortium to Establish a Registry for Alzheimer’s Disease, a modification of the Khachaturian protocol (Khachaturian, 1985).”
MethodHeussen, C., & Dowdle, E. B. (1980) · Analytical Biochemistry · doi:10.1016/0003-2697(80)90338-3 · Cited by 1,989
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor
Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403
Wilhelm, S. M., Collier, I. E., Marmer, B. L., Eisen, A. Z., Grant, G. A., & Goldberg, G. I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71480-4 · Cited by 1,109
Tanzi, R. E., McClatchey, A. I., Lamperti, E. D., Villa‐Komaroff, L., Gusella, J. F., & Neve, R. L. (1988) · Nature · doi:10.1038/331528a0 · Cited by 1,093
Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
Kitaguchi, N., Takahashi, Y., Tokushima, Y., Shiojiri, S., & Ito, H. (1988) · Nature · doi:10.1038/331530a0 · Cited by 1,083
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
Ponte, P. A., Gonzalez‐DeWhitt, P. A., Schilling, J., Miller, J., Hsu, D. K., Greenberg, B., Davis, K. L., Wallace, W., Lieberburg, I. M., Fuller, F. H., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,050
Research works printed but not linked: 3
- 10.1016/0003-2697(87)90021-2 · DOI
- Davis, 1990, A latent M r 94,000 gelatin-degrading metalloproteinase induced during differentiation of HL-60 promyelocytic leukemia cells: a member of the collagenase family of enzymes., Cancer Res, 50, 1113
- Potter H Abraham CR Dressler D (1991) The Alzheimer amyloid components α1-antichymotrypsin and β-protein form a stable complex in vitro. in Alzheimer’s disease: basic mechanisms, diagnosis, and therapeutic strategies, eds Iqbal K McLachlan DRC Winblad B Wisniewski HM (Wiley, New York), pp 275–279.
Cited by
Sorted by citations
Items 201–300 of 337
Lee, S. Y., Kim, H. J., Lee, W. J., Joo, S. H., Jeon, S.-J., Kim, J., Kim, H. S., Han, S., Lee, J., Park, S. H., et al. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9737-2 · Cited by 34
“In contrast, MMP-9 has been implicated in the clearance of Ab peptide and amyloid plaques [ 6 , 59].”
Kurata, T., Kawai, H., Miyazaki, K., Kozuki, M., Morimoto, N., Ohta, Y., Ikeda, Y., & Abe, K. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.06.011 · Cited by 31
“MMP-9 levels are increased in neurons of AD patients [34].”
BackgroundOu-Yang, M.-H., & Van Nostrand, W. E. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-134 · Cited by 30
“In regards to Aβ-degrading enzymes, MMP-2 and MMP-9 are distinctive in that both can degrade soluble Aβ peptides and fibrillar plaque Aβ [74-78].”
BackgroundAnalysis of the Relationship Between Metalloprotease-9 and Tau Protein in Alzheimer’s Disease
Hernándes‐Alejandro, M., Montaño, S., Harrington, C. R., Wischik, C. M., Salas‐Casas, A., Cortés‐Reynosa, P., Salazar, E. P., Cázares-Ápatiga, J., Apátiga-Pérez, R., Ontiveros‐Torres, M. Á., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200146 · Cited by 30
“MMP-9 mRNA is expressed in pyramidal neurons and the active form of the enzyme has been detected in close proximity to extracellular amyloid plaque [24].”
Kurata, T., Miyazaki, K., Kozuki, M., Morimoto, N., Ohta, Y., Ikeda, Y., & Abe, K. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.09.030 · Cited by 31
Bejoy, J., Song, L., Wang, Z., Sang, Q. A., Zhou, Y., & Li, Y. (2018) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.8b00021 · Cited by 31
Impaired brain plasticity as a potential therapeutic target for treatment and prevention of dementia
Rajji, T. K. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1550074 · Cited by 30
ACE variants and risk of intracerebral hemorrhage recurrence in amyloid angiopathy
Domingues‐Montanari, S., Hernández‐Guillamón, M., Fernández‐Cadenas, I., Mendióroz, M., Boada, M., Munuera, J., Rovira, À., Maisterra, O., Parés, M., Gutierrez, M., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.01.019 · Cited by 31
“, 2005) or with -amyloid degradation such as MMPs (Backstrom et al., 1996; Roher et al., 1994), neprilysin (Clarimon et al.”
BackgroundShibata, N., Ohnuma, T., Higashi, S., Usui, C., Ohkubo, T., Kitajima, A., Ueki, A., Nagao, M., & Arai, H. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.09.004 · Cited by 29
“Matrix metalloproteinases (MMPs) are, zinc dependent enzymes, which play a role in the degradation of A [2,18,19].”
BackgroundImplication of matrix metalloproteinases in regulating neuronal disorder
Mukherjee, A. K., & Swarnakar, S. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3752-y · Cited by 27
Yang, C.-N., Wu, M.-F., Liu, C.-C., Jung, W.-H., Chang, Y.-C., Lee, W.-P., Shiao, Y.-J., Wu, C.-L., Liou, H.-H., Lin, S.-K., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx278 · Cited by 27
Regulation of MMP-9 by p53 in first trimester cytotrophoblastic cells
Cohen, M., Wuillemin, C., Irion, O. P., & Bischof, P. (2008) · Human Reproduction · doi:10.1093/humrep/den264 · Cited by 27
“, 2003; Kuzuya and Iguchi, 2003) and degenerative diseases (Backstrom et al., 1996), tumour invasion (Polette et al.”
BackgroundRingland, C., Schweig, J. E., Paris, D., Shackleton, B., Lynch, C., Eisenbaum, M., MULLAN, M. J., Crawford, F., Abdullah, L. I., & Bachmeier, C. J. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.06.018 · Cited by 27
“This observation coincides with prior reporting that MMP-9 levels were increased in AD plasma and brain parenchyma (Backstrom et al., 1996; Lorenzl et al., 2008, 2003).”
ResultThe role of matrix metalloproteinase-9 in dementia
Helbecque, N., Hermant, X., Cottel, D., & Amouyel, P. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00905-4 · Cited by 26
Computational study of effective matrix metalloproteinase 9 (MMP9) targeting natural inhibitors
Liu, N., Wang, X., Wu, H., Lv, X., Xie, H., Guo, Z., Wang, J., Dou, G., Zhang, C., & Sun, M. (2021) · Aging · doi:10.18632/aging.203581 · Cited by 25
Wang, Z., Tang, X., Swaminathan, S. K., Kandimalla, K. K., & Kalari, K. R. (2022) · npj Systems Biology and Applications · doi:10.1038/s41540-022-00235-8 · Cited by 24
Morelli, L., Llovera, R. E., Ibendahl, S., & Castaño, E. M. (2002) · Neurochemical Research · doi:10.1023/a:1021679817756 · Cited by 25
“Moreover, in AD, MMP-9 localized to neuritic plaques and a latent form of the enzyme was shifted to an insoluble compartment (90).”
BackgroundMethodHussain, A. A., Lee, Y., & Marshall, J. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.100775 · Cited by 26
β-lactam antibiotics to tame down molecular pathways of Alzheimer's disease
Kumari, S., & Deshmukh, R. R. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173877 · Cited by 24
Marine Natural Products from the Russian Pacific as Sources of Drugs for Neurodegenerative Diseases
Khotimchenko, Y. S., Silachev, D. N., & Katanaev, V. L. (2022) · Marine Drugs · doi:10.3390/md20110708 · Cited by 25
Ganguly, K., Adhikary, K., Acharjee, A., Acharjee, P., Trigun, S. K., Mutlaq, A. S., Ashique, S., Yasmin, S., Alshahrani, A. M., & Ansari, M. Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135967 · Cited by 23
Jalkute, C. B., Barage, S. H., & Sonawane, K. D. (2015) · RSC Advances · doi:10.1039/c4ra09354b · Cited by 23
Park, S. M., & Kim, K. S. (2013) · Prion · doi:10.4161/pri.22850 · Cited by 23
Brzdąk, P., Nowak, D., Wiera, G., & Mozrzymas, J. W. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00178 · Cited by 21
“…Aβ have been identified in vitro: MMP2 (Roher et al., 1994), plasmin (Ledesma et al., 2000), endothelin-converting enzyme (ECE; Eckman et al., 2001), insulin-degrading enzyme (IDE; Kurochkin and Goto, 1994), neprilysin (NEP; Howell et al., 1995) and MMP-9 (Backstrom et al., 1996; Yan et al., 2006).”
BackgroundLiu, W., Yamashita, T., Kurata, T., Kono, S., Hishikawa, N., Deguchi, K., Zhai, Y., & Abe, K. (2015) · Neurological Research · doi:10.1179/1743132815y.0000000002 · Cited by 21
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Wang, H.-Z., Bi, R., Zhang, D., Li, G., Ma, X., Fang, Y., Li, T., Zhang, C., & Yao, Y. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9411-z · Cited by 21
Sex-specific associations of matrix metalloproteinases in Alzheimer’s disease
Aksnes, M., Edwin, T. H., Saltvedt, I. T., Eldholm, R. S., Chaudhry, F. A., Halaas, N. B., Myrstad, M., Watne, L. O., & Knapskog, A. (2023) · Biology of Sex Differences · doi:10.1186/s13293-023-00514-x · Cited by 20
“Indeed, MMPs are involved in Aβ degradation [11, 12], and MMPs have been found expressed in Aβ plaques [13, 14].”
BackgroundMMP-7 cleaves amyloid β fragment peptides and copper ion inhibits the degradation
Taniguchi, M., Matsuura, K., Nakamura, R., Kojima, A., Konishi, M., & Akizawa, T. (2017) · BioMetals · doi:10.1007/s10534-017-0048-4 · Cited by 21
Matrix metalloproteinase 3 haplotypes and plasma amyloid beta levels: The Rotterdam Study
Reitz, C., van Rooij, F. J. A., Soares, H. D., de Maat, M. P. M., Albert Hofman, D., Witteman, J. C. M., & Breteler, M. M. B. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.05.033 · Cited by 21
Fisher, K. E., Fei, Q., Laird, E. R., Stock, J. L., Allen, M. R., Sahagan, B. G., & Strick, C. A. (2002) · Biochemistry · doi:10.1021/bi012076t · Cited by 20
Maeda, M., Vanlandingham, B. D., Ye, H., Lu, P. C.-S., & Azar, D. T. (1998) · Current Eye Research · doi:10.1076/ceyr.17.8.836.5155 · Cited by 20
Pirici, D. N., Pirici, I., Mogoantă, L., Mărgăritescu, O. C., Tudorică, V., Mărgăritescu, C., Ion, D. A., Simionescu, C. E., & Coconu, M. (2011) · Neuropathology · doi:10.1111/j.1440-1789.2011.01279.x · Cited by 19
“Although it has been shown that MMP-9 synthesized by pyramidal neurons in the hippocampus is able to process amyloid Ab1-40 peptide, no nuclear localization of MMP-9 could be observed for any hippocampal area.(36) The few studies available addressing the function of nuclear neuronal or non-neuronal MMPs suggest a role…”
BackgroundHussain, A. A., Lee, Y., Zhang, J.-J., Francis, P. T., & Marshall, J. (2017) · Journal of Neurodegenerative Diseases · doi:10.1155/2017/4810232 · Cited by 20
Reiss, M. J., Han, Y., & Garner, W. L. (2009) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2009.00476.x · Cited by 19
“exogenous chemical activator, activated MMP-9 has been shown to degrade amyloid deposits in the brain.(39,40) The imbalance in MMPs and their inhibitors may lead to many pathologic circumstances.”
BackgroundMurakami, K., Watanabe, T., Koike, T., Kamata, M., Igari, T., & Kondo, S. (2015) · Brain Research · doi:10.1016/j.brainres.2015.12.016 · Cited by 18
Marine pharmacology: therapeutic targeting of matrix metalloproteinases in neuroinflammation
Gentile, E., & Liuzzi, G. M. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.09.023 · Cited by 19
Achilli, C., Ciana, A., & Minetti, G. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2178-0 · Cited by 18
Amyloid β Degradation: A Challenging Task for Brain Peptidases
Morelli, L., Bulloj, A., Leal, M. C., & Castaño, E. M. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_6 · Cited by 18
Porter, K. N., Sarkar, S. N., Dakhlallah, D. A., Vannoy, M. E., Quintana, D. D., & Simpkins, J. W. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00092 · Cited by 17
“MPA promotes changes in the circulating levels of matrix metalloproteinases (MMPs), such as MMP-9, in the endometrium, yet limited literature studying the effects of MPA on neurons and astroglia cells has been conducted.”
BackgroundResultInfluentialExperimental approaches for altering the expression of Abeta‐degrading enzymes
Loeffler, D. A. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15762 · Cited by 18
“…et al., 2001]), the percentage of MMP- 9 that was in a latent (inactive) form was found to be higher in AD brain than in control brain specimens (Backstrom et al., 1996), suggesting that despite MMP's association with plaques, it may not be able to effectively degrade these fibrillar Aβ…”
BackgroundAzargoonjahromi, A. (2024) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgae066 · Cited by 17
Griswold, A. J., Sivasankaran, S. K., Booven, D. V., Gardner, O. K., Rajabli, F., Whitehead, P. L., Hamilton‐Nelson, K. L., Adams, L. D., Scott, A. M., Hofmann, N. K., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-190855 · Cited by 19
Interacting partners of macrophage-secreted cathepsin B contribute to HIV-induced neuronal apoptosis
Cantres-Rosario, Y. M., Hernández, N. C., Negrón, K., Laspiur, J. P., Leszyk, J., Shaffer, S. A., & Meléndez, L. M. (2015) · AIDS · doi:10.1097/qad.0000000000000823 · Cited by 17
Altered TIMP-3 Levels in the Cerebrospinal Fluid and Plasma of Patients with Alzheimer’s Disease
Park, J., Cho, S., Jo, C., Park, M. H., Han, C., Kim, E., Huh, G. Y., & Koh, Y. H. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12050827 · Cited by 15
“It has been already reported that MMPs are elevated in the postmortem brains of AD patients [8,9].”
BackgroundProteases Upregulation in Sporadic Alzheimer’s Disease Brain
Medoro, A., Bartollino, S., Mignogna, D., Marziliano, N., Porcile, C., Nizzari, M., Florio, T., Pagano, A., Raimo, G., Intrieri, M., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181284 · Cited by 20
Amyloid beta peptide-degrading microbial enzymes and its implication in drug design
Dhanavade, M. J., & Sonawane, K. D. (2020) · 3 Biotech · doi:10.1007/s13205-020-02240-2 · Cited by 16
Patel, A., Vasanthan, V., Fu, W., Fahlman, R. P., MacTavish, D., & Jhamandas, J. H. (2015) · Brain Structure and Function · doi:10.1007/s00429-015-1007-x · Cited by 19
“These results are consistent with studies in non-neuronal tissues, where histamine H 1 R antagonists blocked the histamine-induced production of MMP-2 and MMP-9 in nasal fibroblasts and human keratinocytes (Asano et al. 2004; Gschwandtner et al. 2008).”
InfluentialChavoshinezhad, S., Beirami, E., & Izadpanah, E. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118568 · Cited by 15
Cañeque‐Rufo, H., Sánchez‐Alonso, M. G., Zuccaro, A., Sevillano, J., Ramos, P., & Herradón, G. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113578 · Cited by 14
Exceptional in vivo catabolism of neurodegeneration-related aggregates
Datki, Z., Galik-Olah, Z., Hortobágyi, T., Mácsai, L., Zsuga, K., Fülöp, L., Bozsó, Z., Gálik, B., Ács, É., Földi, A., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0507-3 · Cited by 14
Beltrán, E., Matiasek, K., Risio, L. D., Stefani, A. D., Feliu‐Pascual, A. L., & Matiasek, L. A. (2013) · Veterinary Pathology · doi:10.1177/0300985813481610 · Cited by 13
“brain.(2,24,29) In humans, however, there were no significant differences in the expression of MMP-9 among different regions of the central nervous system.”
BackgroundAmontree, M., Nelson, M., Stefansson, L., Pak, D. T. S., Maguire-Zeiss, K., Turner, R., & Conant, K. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16031 · Cited by 13
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Leite, J. P., & Gales, L. (2018) · FEBS Letters · doi:10.1002/1873-3468.13285 · Cited by 12
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Tanskanen, M., Myllykangas, L., Saarialho‐Kere, U., & Paetau, A. E. (2011) · Amyloid · doi:10.3109/13506129.2010.541960 · Cited by 12
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“MMP2 and MMP9 are known to degrade A (cid:2) [54, 55].”
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Gasche, Y. G., & Copin, J. C. (2003) · Annales Françaises d Anesthésie et de Réanimation · doi:10.1016/s0750-7658(03)00069-8 · Cited by 12
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Torsello, A., Bresciani, E., Ravelli, M., Rizzi, L., Bulgarelli, I., Ricci, G., Ghiazza, B., Puppo, M. D., Mainini, V., Omeljaniuk, R. J., et al. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.06.006 · Cited by 12
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Choi, H. S., Kim, E., Choi, J. Y., Park, E., & Lee, H. J. (2021) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.12390 · Cited by 11
Kumar, V. S. (2023) · Brain Circulation · doi:10.4103/bc.bc_95_22 · Cited by 11
Matrix metalloproteinase 3 haplotypes and dementia and Alzheimer's disease
Reitz, C., van Rooij, F. J. A., de Maat, M. P. M., den Heijer, T., Albert Hofman, D., Witteman, J. C. M., & Breteler, M. M. B. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.01.001 · Cited by 11
Chapter 6 Reperfusion injury after stroke: neurovascular proteases and the blood–brain barrier
Ning, M., Wang, X., & Lo, E. H. (2008) · Handbook of clinical neurology · doi:10.1016/s0072-9752(08)01906-4 · Cited by 10
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Musunuri, S., Kultima, K., Richard, B. C., Ingelsson, M., Lannfelt, L., Bergquist, J., & Shevchenko, G. (2014) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-014-8320-8 · Cited by 8
The functional MMP-9 microsatellite marker is not associated with episodic memory in humans
Vassos, E., Ma, X., Fiotti, N., Wang, Q., Sham, P. C., Liu, X., Wang, Y., Yan, C., Meng, H., Deng, W., et al. (2008) · Psychiatric Genetics · doi:10.1097/ypg.0b013e3283053009 · Cited by 8
“It is synthesized in neurons of the human hippocampus (Backstrom et al., 1996), and plays an important role in synaptic plasticity and hippocampal-dependent learning (Meighan et al.”
BackgroundWang, X., Li, B., Yu, X., Zhou, Y., Wang, K., & Gao, Y. (2023) · Molecular Medicine Reports · doi:10.3892/mmr.2023.13139 · Cited by 7
“…increased the mrna expression levels of MMP‑3 and MMP‑9, which are located around amyloid plaques and elevated in the brain of patients with ad (54,55). in the ra2 microglia cell line, excessive a β accumulation elevated the activity of MMP‑3 and subsequently activated PI3K/Akt signaling…”
Datki, Z., Balazs, E., Gálik, B., Sinka, R., Zeitler, L., Bozsó, Z., Kalman, J. L., Hortobágyi, T., & Galik-Olah, Z. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.12.184 · Cited by 6
Gonçalves, N. P., Gonçalves, P., Magalhães, J., Ventosa, M., Coelho, A. V., & Saraiva, M. J. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.07.020 · Cited by 9
Ms4a4a deficiency ameliorates plaque pathology in a mouse model of amyloid accumulation
Danhash, E., Verbeck, A. C., Western, D., Díaz‐Pacheco, A. S., Galasso, G., You, S., Huang, G., Starr, E., Miller, N., Nadarajah, C. J., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70580 · Cited by 6
Iemmolo, M., Bivona, G., Piccoli, T., Nicosia, A., Schiera, G., Liegro, C. M. D., Pietra, F. D., & Ghersi, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052510 · Cited by 6
The NGF Metabolic Pathway: New Opportunities for Biomarker Research and Drug Target Discovery
Pentz, R., & Iulita, M. F. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-74046-7_4 · Cited by 7
Zinc and Alzheimer's Disease: An Update
Cuajungco, M. P., Lees, G. J., Kydd, R. R., Tanzi, R. E., & Bush, A. I. (1999) · Nutritional Neuroscience · doi:10.1080/1028415x.1999.11747277 · Cited by 6
Computational Approaches to Understand Cleavage Mechanism of Amyloid Beta (Aβ) Peptide
Sonawane, K. D., & Dhanavade, M. J. (2017) · Neuromethods · doi:10.1007/978-1-4939-7404-7_11 · Cited by 7
Fukami, S., Iwata, N., & Saido, T. C. (2002) · Drug Development Research · doi:10.1002/ddr.10073 · Cited by 5
“Several possible cleavage sites to be attacked by various peptidases, such as gelatinase A [Yamada et al., 1995], gelatinase B [Backstrom et al., 1996], neprilysin [Howell et al., 1995], insulin-degrading enzyme (IDE) [Qiu et al., 1998], cathepsin D [Hamazaki, 1996], metalloendopeptidase [Carvalho…”
Chinnappan, R., Ramachandran, L., Uttam, I., Citartan, M., Ballal, N. V., & Mani, N. K. (2025) · Biosensors · doi:10.3390/bios15090603 · Cited by 5
“It also plays an essential role in basement membrane degradation [50–54].”
No influence of amyloid-β-degrading neprilysin activity on prion pathogenesis
Glatzel, M., Mohajeri, M. H., Poirier, R., Nitsch, R. M., Schwarz, P., Lu, B., & Aguzzi, A. (2005) · Journal of General Virology · doi:10.1099/vir.0.80811-0 · Cited by 5
“Indeed, studies focusing on possible substrates of metalloproteases provided evidence that matrix metalloprotease MMP-9 is able to degrade amyloid-b and might possess PrPScdegrading properties (Backstrom et al., 1996).”
BackgroundClassification, pathology, and basic aspects
Pantoni, L., & Gorelick, P. B. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781139382694.002 · Cited by 5
Kays, M., Kelly, A. M., McGinnis, F., Woods, C., Herron, E., Brown, C. M., & Coulibaly, A. P. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1672768 · Cited by 5
Recent Molecular Targets and their Ligands for the Treatment of Alzheimer Disease
Bayraktar, G., & Alptüzün, V. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266318722240809050235 · Cited by 4
Bouisset, G., Tixier, F. J., Dupak, T., Lejards, C., & Verret, L. (2025) · iScience · doi:10.1016/j.isci.2025.113344 · Cited by 4
Matrix metalloproteinases in neuro-inflammatory disease
Gearing, A. J. H., Adams, S. E., Clements, J., & Miller, K. (1999) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8666-6_4 · Cited by 4
Saraiva, M. J., Guimarães, A., Sousa, M. M., & do Amaral, B. (2004) · CRC Press eBooks · doi:10.1201/9781420037494.ch109 · Cited by 4
Matrix Metallopeptidase 9/Gelatinase B
Eisen Arthur, Z., Sarkar Susanta, K., Neuman, K. C., & Goldberg, G. I. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382219-2.00157-5 · Cited by 4
Ng, B., Kodosaki, E., Veleva, E., Keshavan, A., Schott, J. M., Heslegrave, A., Fox, N. C., & Zetterberg, H. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71082 · Cited by 3
“42,43 On the other hand, OPN levels were reported to be elevated in macrophages engaged in A β clearance whereasthepharmacologicalinhibitionofOPNimpairstheirA β uptake ability.”
Degradation of pathogenic amyloids induced by matrix metalloproteinase-9
Stepanenko, O. V., Sulatsky, M. I., Mikhailova, E. V., Stepanenko, O. V., & Sulatskaya, A. I. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136362 · Cited by 3
The role of metalloproteinases on blood-brain barrier breakdown after ischemic stroke
Gasche, Y. G., Copin, J., & Chan, P. H. (2001) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8297-2_20 · Cited by 3
The link between large artery aging and cerebral small vessel disease
Scuteri, A., & Lakatta, E. G. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781139382694.010 · Cited by 3
Leissring, M. A., & Saido, T. C. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_10 · Cited by 3
Inui, T., Hoffer, M. E., & Balaban, C. D. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147541 · Cited by 3
Beta Amyloid Protein Clearance and Microglial Activation
Frautschy, S. A., Cole, G. M., & Ard, M. D. (2002) · Springer eBooks · doi:10.1007/978-1-4757-4139-1_12 · Cited by 3
Kieseier, B. C., Storch, M. K., & Hartung, H. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6781-6_10 · Cited by 3
Mo, Y., Zhang, X., Lao, Y.-G., Wang, B., Li, X., Zheng, Y., & Ding, W. (2022) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2022.2082304 · Cited by 2
“Besides, MMP9 can degrade extracellular domains of some cell membrane proteins [16], and cleave some proteins in extracellular environment or working as intracellular substrates [17,18], which indicates that MMP9 affects cell status and intercellular relation through regulating proteins.”
BackgroundType IV Collagenases and Blood-Brain Barrier Breakdown in Brain Ischemia
Gasche, Y. G., Copin, J., & Chan, P. H. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-297-5_11 · Cited by 2
A review of plant-derived products regulating amyloid beta-degrading enzymes in Alzheimer’s disease
Honaramouz, B., Imenshahidi, M., & Hosseinzadeh, H. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158053 · Cited by 1
Cell-type-specific APOE4 cascade across the Alzheimer’s disease continuum
Shostak, D. M., Liang, Z., & Huang, Y. (2026) · Neuron · doi:10.1016/j.neuron.2026.04.024 · Cited by 1
Multifaceted Role of Matrix Metalloproteases on Human Diseases
Roy, S., Pramanik, A., Chakraborti, T., & Chakraborti, S. (2017) · Springer eBooks · doi:10.1007/978-981-10-3162-5_2 · Cited by 2
Ikezu, T. (2016) · Springer eBooks · doi:10.1007/978-3-319-44022-4_30 · Cited by 1
Metadata
- Authors
- Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A.
- Affiliations
- University of Southern California (US)
- ORCID
- Cullen, Michael J.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1996-12-15
- Volume
- 16
- Issue
- 24
- Pages
- 7910-7919
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W4296941341
- Cited by
- 331
- References
- 46
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 9 · 2023: 6 · 2022: 10 · 2021: 16 · 2020: 21 · 2019: 5 · 2018: 13 · 2017: 15 · 2016: 11 · 2015: 18 · 2014: 18 · 2013: 8 · 2012: 12
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Funders
- National Institute on Aging (R01-AG09681)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- MMP-9, Alzheimer's disease, Aβ40, hippocampal pyramidal neurons, MMP-9 mRNA expression, extracellular matrix metalloproteinases, transmembrane domain
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